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Long-chain fatty acid transport protein 4 (FATP-4) (Fatty acid transport protein 4) (EC 6.2.1.-) (Solute carrier family 27 member 4)

 S27A4_MOUSE             Reviewed;         643 AA.
Q91VE0; O88562; Q3TD48;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
23-MAY-2018, entry version 140.
RecName: Full=Long-chain fatty acid transport protein 4;
Short=FATP-4;
Short=Fatty acid transport protein 4;
EC=6.2.1.-;
AltName: Full=Solute carrier family 27 member 4;
Name=Slc27a4; Synonyms=Acsvl4, Fatp4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=11404000; DOI=10.1016/S0378-1119(01)00489-9;
Herrmann T., Buchkremer F., Gosch I., Hall A.M., Bernlohr D.A.,
Stremmel W.;
"Mouse fatty acid transport protein 4 (FATP4): characterization of the
gene and functional assessment as a very long chain acyl-CoA
synthetase.";
Gene 270:31-40(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Vagina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
Mollenhauer J., Wiemann S., Schick M., Korn B.;
"Cloning of mouse full open reading frames in Gateway(R) system entry
vector (pDONR201).";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 145-643, AND TISSUE SPECIFICITY.
PubMed=9671728; DOI=10.1073/pnas.95.15.8625;
Hirsch D., Stahl A., Lodish H.F.;
"A family of fatty acid transporters conserved from mycobacterium to
man.";
Proc. Natl. Acad. Sci. U.S.A. 95:8625-8629(1998).
[6]
FUNCTION IN FATTY ACID TRANSPORT, AND TISSUE SPECIFICITY.
PubMed=10518211; DOI=10.1016/S1097-2765(00)80332-9;
Stahl A., Hirsch D.J., Gimeno R.E., Punreddy S., Ge P., Watson N.,
Patel S., Kotler M., Raimondi A., Tartaglia L.A., Lodish H.F.;
"Identification of the major intestinal fatty acid transport
protein.";
Mol. Cell 4:299-308(1999).
[7]
TISSUE SPECIFICITY.
PubMed=14512415; DOI=10.1074/jbc.M309759200;
Gimeno R.E., Hirsch D.J., Punreddy S., Sun Y., Ortegon A.M., Wu H.,
Daniels T., Stricker-Krongrad A., Lodish H.F., Stahl A.;
"Targeted deletion of fatty acid transport protein-4 results in early
embryonic lethality.";
J. Biol. Chem. 278:49512-49516(2003).
[8]
FUNCTION.
PubMed=12821645; DOI=10.1083/jcb.200207080;
Herrmann T., van der Hoeven F., Grone H.J., Stewart A.F., Langbein L.,
Kaiser I., Liebisch G., Gosch I., Buchkremer F., Drobnik W.,
Schmitz G., Stremmel W.;
"Mice with targeted disruption of the fatty acid transport protein 4
(Fatp 4, Slc27a4) gene show features of lethal restrictive
dermopathy.";
J. Cell Biol. 161:1105-1115(2003).
[9]
DISEASE.
PubMed=12697906; DOI=10.1073/pnas.0431186100;
Moulson C.L., Martin D.R., Lugus J.J., Schaffer J.E., Lind A.C.,
Miner J.H.;
"Cloning of wrinkle-free, a previously uncharacterized mouse mutation,
reveals crucial roles for fatty acid transport protein 4 in skin and
hair development.";
Proc. Natl. Acad. Sci. U.S.A. 100:5274-5279(2003).
[10]
FUNCTION AS AN ACYL-COA LIGASE.
PubMed=15653672; DOI=10.1074/jbc.M412629200;
Hall A.M., Wiczer B.M., Herrmann T., Stremmel W., Bernlohr D.A.;
"Enzymatic properties of purified murine fatty acid transport protein
4 and analysis of acyl-CoA synthetase activities in tissues from FATP4
null mice.";
J. Biol. Chem. 280:11948-11954(2005).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15699031; DOI=10.1074/jbc.M409598200;
DiRusso C.C., Li H., Darwis D., Watkins P.A., Berger J., Black P.N.;
"Comparative biochemical studies of the murine fatty acid transport
proteins (FATP) expressed in yeast.";
J. Biol. Chem. 280:16829-16837(2005).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=23407971; DOI=10.1523/JNEUROSCI.2428-12.2013;
Li S., Lee J., Zhou Y., Gordon W.C., Hill J.M., Bazan N.G.,
Miner J.H., Jin M.;
"Fatty acid transport protein 4 (FATP4) prevents light-induced
degeneration of cone and rod photoreceptors by inhibiting RPE65
isomerase.";
J. Neurosci. 33:3178-3189(2013).
-!- FUNCTION: Involved in translocation of long-chain fatty acids
(LFCA) across the plasma membrane. Appears to be the principal
fatty acid transporter in small intestinal enterocytes. Plays a
role in the formation of the epidermal barrier. Required for fat
absorption in early embryogenesis. Has acyl-CoA ligase activity
for long-chain and very-long-chain fatty acids (VLCFAs).
Indirectly inhibits RPE65 via substrate competition and via
production of VLCFA derivatives like lignoceroyl-CoA. Prevents
light-induced degeneration of rods and cones.
{ECO:0000269|PubMed:10518211, ECO:0000269|PubMed:11404000,
ECO:0000269|PubMed:12821645, ECO:0000269|PubMed:15653672,
ECO:0000269|PubMed:15699031, ECO:0000269|PubMed:23407971}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}. Endoplasmic reticulum membrane.
-!- TISSUE SPECIFICITY: Most abundantly expressed in small intestine,
brain, kidney, liver, skin and heart. In small intestine,
expressed at high levels on the apical side of mature enterocytes.
Highly expressed by the epithelial cells of the visceral endoderm
and localized to the brush-border membrane of extraembryonic
endodermal cells (at protein level). Expressed in the retinal
pigment epithelium and in the retina (at protein level). Expressed
in the retinal pigment epithelium and in the retina.
{ECO:0000269|PubMed:10518211, ECO:0000269|PubMed:11404000,
ECO:0000269|PubMed:14512415, ECO:0000269|PubMed:23407971,
ECO:0000269|PubMed:9671728}.
-!- DISEASE: Note=Defects in Slc27a4 are the cause of wrinkle-free
(wrfr) phenotype. It is a spontaneous, autosomal recessive
mutation resulting in very tight, thick skin and is secondary
characterized by severe breathing difficulties. Mice die shortly
after birth. This phenotype is similar to human restrictive
dermopathy, a very rare human genetic disorder.
{ECO:0000269|PubMed:12697906}.
-!- MISCELLANEOUS: Slc27a4 deficient mice display features of a
neonatally lethal restrictive dermopathy. Their skin is
characterized by hyperproliferative hyperkeratosis with a
disturbed epidermal barrier, a flat dermal-epidermal junction, a
reduced number of pilo-sebaceous structures, and a compact dermis.
The rigid skin consistency results in an altered body shape with
facial dysmorphia, generalized joint flexion contractures and
impaired movement including suckling and breathing deficiencies.
Lipid analysis demonstrates a disturbed fatty acid composition of
epidermal ceramides, in particular a decrease in the C26:0 and
C26:0-OH fatty acid substitutes.
-!- MISCELLANEOUS: Deletion of Slc27a4 results in embryonic lethality,
which has been attributed to a requirement for fat absorption
early in embryonic development across the visceral endoderm.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC40188.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=AAC40188.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AJ251113; CAC42082.1; -; mRNA.
EMBL; AJ276492; CAC42083.1; -; Genomic_DNA.
EMBL; AK036919; BAC29639.1; -; mRNA.
EMBL; AK155388; BAE33236.1; -; mRNA.
EMBL; AK170377; BAE41756.1; -; mRNA.
EMBL; CT010312; CAJ18520.1; -; mRNA.
EMBL; BC023114; AAH23114.1; -; mRNA.
EMBL; AF072759; AAC40188.1; ALT_SEQ; mRNA.
CCDS; CCDS15858.1; -.
RefSeq; NP_036119.1; NM_011989.4.
UniGene; Mm.330113; -.
ProteinModelPortal; Q91VE0; -.
BioGrid; 205025; 1.
STRING; 10090.ENSMUSP00000078971; -.
SwissLipids; SLP:000001141; -.
TCDB; 4.C.1.1.1; the fatty acid transporter (fat) family.
iPTMnet; Q91VE0; -.
PhosphoSitePlus; Q91VE0; -.
SwissPalm; Q91VE0; -.
MaxQB; Q91VE0; -.
PaxDb; Q91VE0; -.
PeptideAtlas; Q91VE0; -.
PRIDE; Q91VE0; -.
Ensembl; ENSMUST00000080065; ENSMUSP00000078971; ENSMUSG00000059316.
GeneID; 26569; -.
KEGG; mmu:26569; -.
UCSC; uc008jaf.1; mouse.
CTD; 10999; -.
MGI; MGI:1347347; Slc27a4.
eggNOG; KOG1179; Eukaryota.
eggNOG; ENOG410XQ8T; LUCA.
GeneTree; ENSGT00550000074420; -.
HOGENOM; HOG000044189; -.
HOVERGEN; HBG005642; -.
InParanoid; Q91VE0; -.
KO; K08745; -.
OMA; FQGYYGN; -.
OrthoDB; EOG091G0B76; -.
PhylomeDB; Q91VE0; -.
TreeFam; TF313430; -.
BRENDA; 6.2.1.3; 3474.
Reactome; R-MMU-804914; Transport of fatty acids.
PRO; PR:Q91VE0; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000059316; -.
Genevisible; Q91VE0; MM.
GO; GO:0031526; C:brush border membrane; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005902; C:microvillus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:MGI.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IDA:MGI.
GO; GO:0006631; P:fatty acid metabolic process; IMP:MGI.
GO; GO:0044539; P:long-chain fatty acid import; ISO:MGI.
GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:MGI.
GO; GO:0015909; P:long-chain fatty acid transport; IMP:MGI.
GO; GO:0001579; P:medium-chain fatty acid transport; IDA:MGI.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0043588; P:skin development; IMP:MGI.
GO; GO:0042760; P:very long-chain fatty acid catabolic process; IDA:MGI.
GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:MGI.
CDD; cd05939; hsFATP4_like; 1.
InterPro; IPR025110; AMP-bd_C.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
InterPro; IPR030304; FATP4.
InterPro; IPR022272; Lipocalin_CS.
PANTHER; PTHR43107:SF11; PTHR43107:SF11; 1.
Pfam; PF00501; AMP-binding; 1.
Pfam; PF13193; AMP-binding_C; 1.
PROSITE; PS00455; AMP_BINDING; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Fatty acid metabolism;
Ligase; Lipid metabolism; Lipid transport; Membrane;
Nucleotide-binding; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 643 Long-chain fatty acid transport protein
4.
/FTId=PRO_0000193211.
TRANSMEM 20 42 Helical. {ECO:0000255}.
TRANSMEM 139 156 Helical. {ECO:0000255}.
NP_BIND 243 254 AMP. {ECO:0000255}.
CONFLICT 330 330 I -> V (in Ref. 5; AAC40188).
{ECO:0000305}.
CONFLICT 542 542 P -> S (in Ref. 2; BAE41756).
{ECO:0000305}.
SEQUENCE 643 AA; 72319 MW; 10B3E9730FDF586A CRC64;
MLLGASLVGA LLFSKLVLKL PWTQVGFSLL LLYLGSGGWR FIRVFIKTVR RDIFGGMVLL
KVKTKVRRYL QERKTVPLLF ASMVQRHPDK TALIFEGTDT HWTFRQLDEY SSSVANFLQA
RGLASGNVVA LFMENRNEFV GLWLGMAKLG VEAALINTNL RRDALRHCLD TSKARALIFG
SEMASAICEI HASLEPTLSL FCSGSWEPST VPVSTEHLDP LLEDAPKHLP SHPDKGFTDK
LFYIYTSGTT GLPKAAIVVH SRYYRMASLV YYGFRMRPDD IVYDCLPLYH SAGNIVGIGQ
CLLHGMTVVI RKKFSASRFW DDCIKYNCTI VQYIGELCRY LLNQPPREAE SRHKVRMALG
NGLRQSIWTD FSSRFHIPQV AEFYGATECN CSLGNFDSRV GACGFNSRIL SFVYPIRLVR
VNEDTMELIR GPDGVCIPCQ PGQPGQLVGR IIQQDPLRRF DGYLNQGANN KKIANDVFKK
GDQAYLTGDV LVMDELGYLY FRDRTGDTFR WKGENVSTTE VEGTLSRLLH MADVAVYGVE
VPGTEGRAGM AAVASPISNC DLESFAQTLK KELPLYARPI FLRFLPELHK TGTFKFQKTE
LRKEGFDPSV VKDPLFYLDA RKGCYVALDQ EAYTRIQAGE EKL


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